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  • Signal Transduction  (23)
  • American Association for the Advancement of Science (AAAS)  (23)
  • Springer Nature
  • 2000-2004  (23)
  • 1995-1999
  • 1980-1984
  • 1970-1974
  • 1940-1944
  • 2004  (23)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (23)
  • Springer Nature
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  • 2000-2004  (23)
  • 1995-1999
  • 1980-1984
  • 1970-1974
  • 1940-1944
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  • 1
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    Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: The development of a patterned vasculature is essential for normal organogenesis. We found that signaling by semaphorin 3E (Sema3E) and its receptor plexin-D1 controls endothelial cell positioning and the patterning of the developing vasculature in the mouse. Sema3E is highly expressed in developing somites, where it acts as a repulsive cue for plexin-D1-expressing endothelial cells of adjacent intersomitic vessels. Sema3E-plexin-D1 signaling did not require neuropilins, which were previously presumed to be obligate Sema3 coreceptors. Moreover, genetic ablation of Sema3E or plexin-D1 but not neuropilin-mediated Sema3 signaling disrupted vascular patterning. These findings reveal an unexpected semaphorin signaling pathway and define a mechanism for controlling vascular patterning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Chenghua -- Yoshida, Yutaka -- Livet, Jean -- Reimert, Dorothy V -- Mann, Fanny -- Merte, Janna -- Henderson, Christopher E -- Jessell, Thomas M -- Kolodkin, Alex L -- Ginty, David D -- CA23767-24/CA/NCI NIH HHS/ -- MH59199-06/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):265-8. Epub 2004 Nov 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550623" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Blood Vessels/*embryology/metabolism ; Body Patterning ; COS Cells ; Cercopithecus aethiops ; Chick Embryo ; Endothelial Cells/cytology/physiology ; Endothelium, Vascular/cytology/embryology ; Glycoproteins/*metabolism ; In Situ Hybridization ; Ligands ; Membrane Glycoproteins/*metabolism ; Membrane Proteins/*metabolism ; Mice ; Morphogenesis ; Mutation ; Nerve Tissue Proteins/*metabolism ; Neuropilin-1/metabolism ; Neuropilin-2/metabolism ; Phenotype ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Somites/*metabolism ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Protein kinase C overactivity impairs prefrontal cortical regulation of working memory (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-30
    Description: The prefrontal cortex is a higher brain region that regulates thought, behavior, and emotion using representational knowledge, operations often referred to as working memory. We tested the influence of protein kinase C (PKC) intracellular signaling on prefrontal cortical cognitive function and showed that high levels of PKC activity in prefrontal cortex, as seen for example during stress exposure, markedly impair behavioral and electrophysiological measures of working memory. These data suggest that excessive PKC activation can disrupt prefrontal cortical regulation of behavior and thought, possibly contributing to signs of prefrontal cortical dysfunction such as distractibility, impaired judgment, impulsivity, and thought disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birnbaum, S G -- Yuan, P X -- Wang, M -- Vijayraghavan, S -- Bloom, A K -- Davis, D J -- Gobeske, K T -- Sweatt, J D -- Manji, H K -- Arnsten, A F T -- AG06036/AG/NIA NIH HHS/ -- P50 MH068789/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):882-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Yale Medical School, 333 Cedar Street, New Haven, CT 06520-8001, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514161" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic alpha-Agonists/pharmacology ; Alkaloids ; Animals ; Benzophenanthridines ; Carbolines/pharmacology ; Electrophysiology ; Enzyme Activation ; Female ; Imidazoles/pharmacology ; Lithium Carbonate/pharmacology ; Macaca mulatta ; Male ; Memory/drug effects/*physiology ; Neurons/drug effects/physiology ; Phenanthridines/pharmacology ; Prefrontal Cortex/enzymology/*physiology ; Protein Kinase C/antagonists & inhibitors/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Adrenergic, alpha-1/physiology ; Signal Transduction ; Stress, Physiological/physiopathology ; Tetradecanoylphorbol Acetate/pharmacology ; Valproic Acid/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Mutational analysis of the tyrosine phosphatome in colorectal cancers (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-25
    Description: Tyrosine phosphorylation, regulated by protein tyrosine phosphatases (PTPs) and kinases (PTKs), is important in signaling pathways underlying tumorigenesis. A mutational analysis of the tyrosine phosphatase gene superfamily in human cancers identified 83 somatic mutations in six PTPs (PTPRF, PTPRG, PTPRT, PTPN3, PTPN13, PTPN14), affecting 26% of colorectal cancers and a smaller fraction of lung, breast, and gastric cancers. Fifteen mutations were nonsense, frameshift, or splice-site alterations predicted to result in truncated proteins lacking phosphatase activity. Five missense mutations in the most commonly altered PTP (PTPRT) were biochemically examined and found to reduce phosphatase activity. Expression of wild-type but not a mutant PTPRT in human cancer cells inhibited cell growth. These observations suggest that the mutated tyrosine phosphatases are tumor suppressor genes, regulating cellular pathways that may be amenable to therapeutic intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Zhenghe -- Shen, Dong -- Parsons, D Williams -- Bardelli, Alberto -- Sager, Jason -- Szabo, Steve -- Ptak, Janine -- Silliman, Natalie -- Peters, Brock A -- van der Heijden, Michiel S -- Parmigiani, Giovanni -- Yan, Hai -- Wang, Tian-Li -- Riggins, Greg -- Powell, Steven M -- Willson, James K V -- Markowitz, Sanford -- Kinzler, Kenneth W -- Vogelstein, Bert -- Velculescu, Victor E -- CA 43460/CA/NCI NIH HHS/ -- CA 57345/CA/NCI NIH HHS/ -- CA 62924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 May 21;304(5674):1164-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sidney Kimmel Comprehensive Cancer Center, Howard Hughes Medical Institute, Johns Hopkins University Medical Institutions, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155950" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; Cell Division ; Codon, Nonsense ; Colorectal Neoplasms/*enzymology/*genetics ; Computational Biology ; *DNA Mutational Analysis ; Exons ; Frameshift Mutation ; Genes, Tumor Suppressor ; Humans ; Kinetics ; Markov Chains ; *Mutation ; Mutation, Missense ; Nerve Tissue Proteins/chemistry/genetics/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 13 ; Protein Tyrosine Phosphatase, Non-Receptor Type 3 ; Protein Tyrosine Phosphatases/chemistry/*genetics/metabolism ; Receptor-Like Protein Tyrosine Phosphatases, Class 5 ; Signal Transduction ; Transfection ; Tyrosine/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Cross-linking cellular prion protein triggers neuronal apoptosis in vivo (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-31
    Description: Neuronal death is a prominent, but poorly understood, pathological hallmark of prion disease. Notably, in the absence of the cellular prion protein (PrPC), the disease-associated isoform, PrPSc, appears not to be intrinsically neurotoxic, suggesting that PrPC itself may participate directly in the prion neurodegenerative cascade. Here, cross-linking PrPC in vivo with specific monoclonal antibodies was found to trigger rapid and extensive apoptosis in hippocampal and cerebellar neurons. These findings suggest that PrPC functions in the control of neuronal survival and provides a model to explore whether cross-linking of PrPC by oligomeric PrPSc can promote neuronal loss during prion infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Solforosi, Laura -- Criado, Jose R -- McGavern, Dorian B -- Wirz, Sebastian -- Sanchez-Alavez, Manuel -- Sugama, Shuei -- DeGiorgio, Lorraine A -- Volpe, Bruce T -- Wiseman, Erika -- Abalos, Gil -- Masliah, Eliezer -- Gilden, Donald -- Oldstone, Michael B -- Conti, Bruno -- Williamson, R Anthony -- AG00080/AG/NIA NIH HHS/ -- AG04342/AG/NIA NIH HHS/ -- AI09484/AI/NIAID NIH HHS/ -- HL63817/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 5;303(5663):1514-6. Epub 2004 Jan 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14752167" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology/*metabolism ; *Apoptosis ; Cell Survival ; Cerebellum/*cytology ; Complement Activation ; Dimerization ; Hippocampus/*cytology ; Immunoglobulin Fab Fragments/immunology/metabolism ; Immunoglobulin G/immunology/metabolism ; In Situ Nick-End Labeling ; Mice ; Mice, Inbred C57BL ; Neural Cell Adhesion Molecules/immunology/metabolism ; Neurons/*physiology ; PrPC Proteins/chemistry/immunology/*metabolism ; Recombinant Proteins/metabolism ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: Microtubule (MT) stabilization is regulated by the small guanosine triphosphate (GTP)-binding protein Rho and its effector, mammalian homolog of Diaphanous (mDia), in migrating cells, but factors responsible for localized stabilization at the leading edge are unknown. We report that integrin-mediated activation of focal adhesion kinase (FAK) at the leading edge is required for MT stabilization by the Rho-mDia signaling pathway in mouse fibroblasts. MT stabilization also involved FAK-regulated localization of a lipid raft marker, ganglioside GM1, to the leading edge. The integrin-FAK signaling pathway may facilitate Rho-mDia signaling through GM1, or through a specialized membrane domain containing GM1, to stabilize MTs in the leading edge of migrating cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palazzo, Alexander F -- Eng, Christina H -- Schlaepfer, David D -- Marcantonio, Eugene E -- Gundersen, Gregg G -- CA87038/CA/NCI NIH HHS/ -- GM 44585/GM/NIGMS NIH HHS/ -- GM 62939/GM/NIGMS NIH HHS/ -- GM 68695/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):836-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764879" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Animals ; Carrier Proteins/metabolism ; Cell Adhesion ; Cell Line ; Cell Membrane/*metabolism ; Cholesterol/metabolism ; Fibronectins/metabolism/pharmacology ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; G(M1) Ganglioside/metabolism ; Glycosylphosphatidylinositols/metabolism ; Integrins/*metabolism ; Membrane Microdomains/*metabolism ; Mice ; Mice, Knockout ; Microtubules/*metabolism/ultrastructure ; NIH 3T3 Cells ; Phosphorylation ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Tubulin/metabolism ; rho GTP-Binding Proteins/*metabolism ; rhoA GTP-Binding Protein/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-31
    Description: Gefitinib (Iressa, Astra Zeneca Pharmaceuticals) is a tyrosine kinase inhibitor that targets the epidermal growth factor receptor (EGFR) and induces dramatic clinical responses in nonsmall cell lung cancers (NSCLCs) with activating mutations within the EGFR kinase domain. We report that these mutant EGFRs selectively activate Akt and signal transduction and activator of transcription (STAT) signaling pathways, which promote cell survival, but have no effect on extracellular signal-regulated kinase signaling, which induces proliferation. NSCLC cells expressing mutant EGFRs underwent extensive apoptosis after small interfering RNA-mediated knockdown of the mutant EGFR or treatment with pharmacological inhibitors of Akt and STAT signaling and were relatively resistant to apoptosis induced by conventional chemotherapeutic drugs. Thus, mutant EGFRs selectively transduce survival signals on which NSCLCs become dependent; inhibition of those signals by gefitinib may contribute to the drug's efficacy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sordella, Raffaella -- Bell, Daphne W -- Haber, Daniel A -- Settleman, Jeffrey -- P01 95281/PHS HHS/ -- New York, N.Y. -- Science. 2004 Aug 20;305(5687):1163-7. Epub 2004 Jul 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Therapeutics, Massachusetts General Hospital Cancer Center and Harvard Medical School, Building 149, 13th Street, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15284455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/pharmacology ; *Apoptosis ; Carcinoma, Non-Small-Cell Lung/drug therapy/*genetics/pathology ; Catalytic Domain ; Cell Line ; Cell Line, Tumor ; Cell Survival ; DNA-Binding Proteins/antagonists & inhibitors/metabolism ; Enzyme Activation ; Humans ; Lung Neoplasms/drug therapy/*genetics/pathology ; Mice ; *Milk Proteins ; Mitogen-Activated Protein Kinases/metabolism ; Mutation ; Mutation, Missense ; Phosphorylation ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; Proto-Oncogene Proteins/antagonists & inhibitors/metabolism ; Proto-Oncogene Proteins c-akt ; Quinazolines/*pharmacology ; RNA, Small Interfering ; Receptor, Epidermal Growth Factor/*genetics/*metabolism ; STAT5 Transcription Factor ; Sequence Deletion ; Signal Transduction ; Trans-Activators/antagonists & inhibitors/metabolism ; Transfection ; Tyrosine/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    A family with severe insulin resistance and diabetes due to a mutation in AKT2 (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-29
    Description: Inherited defects in signaling pathways downstream of the insulin receptor have long been suggested to contribute to human type 2 diabetes mellitus. Here we describe a mutation in the gene encoding the protein kinase AKT2/PKBbeta in a family that shows autosomal dominant inheritance of severe insulin resistance and diabetes mellitus. Expression of the mutant kinase in cultured cells disrupted insulin signaling to metabolic end points and inhibited the function of coexpressed, wild-type AKT. These findings demonstrate the central importance of AKT signaling to insulin sensitivity in humans.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2258004/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2258004/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉George, Stella -- Rochford, Justin J -- Wolfrum, Christian -- Gray, Sarah L -- Schinner, Sven -- Wilson, Jenny C -- Soos, Maria A -- Murgatroyd, Peter R -- Williams, Rachel M -- Acerini, Carlo L -- Dunger, David B -- Barford, David -- Umpleby, A Margot -- Wareham, Nicholas J -- Davies, Huw Alban -- Schafer, Alan J -- Stoffel, Markus -- O'Rahilly, Stephen -- Barroso, Ines -- 078986/Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2004 May 28;304(5675):1325-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2QQ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166380" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Adipocytes/cytology/metabolism ; Adult ; Aged ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Catalytic Domain ; Cell Differentiation ; Cell Line ; Cell Nucleus/metabolism ; Cytosol/metabolism ; DNA-Binding Proteins/metabolism ; Diabetes Mellitus/*genetics/metabolism ; Female ; Genes, Dominant ; Hepatocyte Nuclear Factor 3-beta ; Humans ; Hyperinsulinism/genetics/metabolism ; Insulin/metabolism ; Insulin Resistance/*genetics ; Lipid Metabolism ; Male ; Middle Aged ; Molecular Sequence Data ; *Mutation, Missense ; Nuclear Proteins/metabolism ; Pedigree ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins c-akt ; Signal Transduction ; *Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    The pathophysiology of mitochondrial cell death (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-03
    Description: In the mitochondrial pathway of apoptosis, caspase activation is closely linked to mitochondrial outer membrane permeabilization (MOMP). Numerous pro-apoptotic signal-transducing molecules and pathological stimuli converge on mitochondria to induce MOMP. The local regulation and execution of MOMP involve proteins from the Bcl-2 family, mitochondrial lipids, proteins that regulate bioenergetic metabolite flux, and putative components of the permeability transition pore. MOMP is lethal because it results in the release of caspase-activating molecules and caspase-independent death effectors, metabolic failure in the mitochondria, or both. Drugs designed to suppress excessive MOMP may avoid pathological cell death, and the therapeutic induction of MOMP may restore apoptosis in cancer cells in which it is disabled. The general rules governing the pathophysiology of MOMP and controversial issues regarding its regulation are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, Douglas R -- Kroemer, Guido -- New York, N.Y. -- Science. 2004 Jul 30;305(5684):626-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA. doug@liai.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15286356" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Disease/*etiology ; Humans ; Intracellular Membranes/*physiology ; Mitochondria/*physiology ; Models, Biological ; Neoplasms/physiopathology ; Permeability ; Proteins/*metabolism ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Signal Transduction ; Viral Proteins/metabolism ; Virus Physiological Phenomena
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Biomedicine. Insulin resistance takes a trip through the ER (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muoio, Deborah M -- Newgard, Christopher B -- New York, N.Y. -- Science. 2004 Oct 15;306(5695):425-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15486283" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Cells, Cultured ; DNA-Binding Proteins/genetics/metabolism ; Endoplasmic Reticulum/*metabolism ; Endoribonucleases ; Enzyme Activation ; Homeostasis ; Humans ; Insulin/*metabolism ; Insulin Receptor Substrate Proteins ; Insulin Resistance/*physiology ; Islets of Langerhans/metabolism ; Liver/metabolism ; Membrane Proteins/metabolism ; Mice ; Mitogen-Activated Protein Kinase 8 ; Mitogen-Activated Protein Kinases/*metabolism ; Muscle, Skeletal/metabolism ; Nuclear Proteins/genetics/metabolism ; Obesity/*metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction ; Transcription Factors ; eIF-2 Kinase/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-31
    Description: Protein tyrosine kinases and phosphatases cooperate to regulate normal immune cell function. We examined the role of PEST domain-enriched tyrosine phosphatase (PEP) in regulating T cell antigen-receptor function during thymocyte development and peripheral T cell differentiation. Although normal naive T cell functions were retained in pep-deficient mice, effector/memory T cells demonstrated enhanced activation of Lck. In turn, this resulted in increased expansion and function of the effector/memory T cell pool, which was also associated with spontaneous development of germinal centers and elevated serum antibody levels. These results revealed a central role for PEP in negatively regulating specific aspects of T cell development and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hasegawa, Kiminori -- Martin, Flavius -- Huang, Guangming -- Tumas, Dan -- Diehl, Lauri -- Chan, Andrew C -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):685-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Genentech, Inc., One DNA Way, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14752163" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoimmunity ; B-Lymphocytes/physiology ; CD4-Positive T-Lymphocytes/immunology/physiology ; CD8-Positive T-Lymphocytes/immunology/physiology ; Cell Cycle ; Gene Targeting ; Germinal Center/physiology ; Hydrogen-Ion Concentration ; Immunoglobulins/blood ; *Immunologic Memory ; Lymphocyte Activation ; Lymphocyte Count ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/metabolism ; Mice ; Mice, Inbred BALB C ; Mice, Transgenic ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 12 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Receptors, Antigen, T-Cell/genetics/immunology ; Signal Transduction ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/*immunology/physiology
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